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Q9UIG0 (BAZ1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase BAZ1B

EC=2.7.10.2
Alternative name(s):
Bromodomain adjacent to zinc finger domain protein 1B
Williams syndrome transcription factor
Williams-Beuren syndrome chromosomal region 10 protein
Williams-Beuren syndrome chromosomal region 9 protein
hWALp2
Gene names
Name:BAZ1B
Synonyms:WBSC10, WBSCR10, WBSCR9, WSTF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association. Ref.7 Ref.8 Ref.9 Ref.12 Ref.17 Ref.18

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.17

Cofactor

Manganese. Ref.17

Subunit structure

Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Subcellular location

Nucleus. Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA. Ref.7 Ref.9

Tissue specificity

Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary.

Developmental stage

Expressed at equal levels in 19-23 weeks old fetal tissues.

Domain

The N-terminal part (1-345), including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity. Ref.10

The bromo domain mediates the specific interaction with acetylated histones. Ref.10

Involvement in disease

BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. Ref.2

Sequence similarities

Belongs to the WAL family. BAZ1B subfamily.

Contains 1 bromo domain.

Contains 1 DDT domain.

Contains 1 PHD-type zinc finger.

Contains 1 WAC domain.

Sequence caution

The sequence AAC97879.1 differs from that shown. Reason: Frameshift at positions 1031, 1042 and 1422.

The sequence AAD04720.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAH65029.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA89210.1 differs from that shown. Reason: Frameshift at position 1478.

Ontologies

Keywords
   Biological processDNA damage
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseWilliams-Beuren syndrome
   DomainBromodomain
Coiled coil
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from direct assay Ref.8. Source: BHF-UCL

DNA replication-dependent nucleosome disassembly

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

cellular response to DNA damage stimulus

Inferred from direct assay Ref.17. Source: UniProtKB

chromatin-mediated maintenance of transcription

Inferred from sequence or structural similarity. Source: BHF-UCL

double-strand break repair

Inferred from sequence or structural similarity. Source: BHF-UCL

heart morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

histone phosphorylation

Inferred from direct assay Ref.17. Source: UniProtKB

nucleosome disassembly

Inferred from direct assay Ref.8. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.17. Source: GOC

positive regulation of receptor activity

Inferred from mutant phenotype Ref.8. Source: GOC

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription, DNA-templated

Non-traceable author statement Ref.3. Source: BHF-UCL

   Cellular_componentWINAC complex

Inferred from direct assay Ref.8. Source: BHF-UCL

centromeric heterochromatin

Inferred from electronic annotation. Source: Ensembl

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay Ref.10. Source: UniProtKB

histone acetyl-lysine binding

Inferred from direct assay Ref.10. Source: UniProtKB

histone kinase activity

Inferred from direct assay Ref.17. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein complex scaffold

Inferred from direct assay Ref.8. Source: BHF-UCL

protein tyrosine kinase activity

Inferred from direct assay Ref.17. Source: UniProtKB

vitamin D receptor activator activity

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

vitamin D receptor binding

Inferred from physical interaction Ref.8. Source: BHF-UCL

zinc ion binding

Non-traceable author statement Ref.22. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMARCA5O602646EBI-927482,EBI-352588

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UIG0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UIG0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     660-663: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14831483Tyrosine-protein kinase BAZ1B
PRO_0000211170

Regions

Domain20 – 126107WAC
Domain604 – 66865DDT
Domain1356 – 142671Bromo
Zinc finger1184 – 123451PHD-type
Region1 – 345345Mediates the tyrosine-protein kinase activity
Coiled coil533 – 58654 Potential
Coiled coil768 – 81447 Potential
Coiled coil850 – 89344 Potential
Coiled coil1245 – 128339 Potential
Motif207 – 2137C motif
Compositional bias306 – 578273Lys-rich
Compositional bias1261 – 127313Poly-Glu

Amino acid modifications

Modified residue1611Phosphoserine By similarity
Modified residue2661Phosphothreonine Ref.20
Modified residue3301Phosphoserine Ref.15
Modified residue3451Phosphoserine Ref.20
Modified residue3471Phosphoserine Ref.20 Ref.21
Modified residue3491Phosphoserine Ref.20 Ref.21
Modified residue3611Phosphoserine Ref.20
Modified residue3741Phosphoserine Ref.15
Modified residue6991Phosphoserine Ref.15
Modified residue7051Phosphoserine Ref.15 Ref.19 Ref.21
Modified residue7081Phosphoserine Ref.15
Modified residue7161Phosphoserine Ref.15
Modified residue9471Phosphoserine Ref.15
Modified residue13151Phosphoserine Ref.15
Modified residue13351N6-acetyllysine By similarity
Modified residue13421Phosphoserine Ref.11 Ref.20 Ref.21
Modified residue14681Phosphoserine Ref.11 Ref.14 Ref.15 Ref.20 Ref.21

Natural variations

Alternative sequence660 – 6634Missing in isoform 2.
VSP_000552

Experimental info

Mutagenesis3381C → A: Loss of tyrosine-protein kinase activity. Ref.17
Sequence conflict141K → N in BAA89210. Ref.3
Sequence conflict221L → F in BAA89210. Ref.3
Sequence conflict1361K → E in AAD08675. Ref.1
Sequence conflict8231E → R in BAA89210. Ref.3
Sequence conflict11911R → P in BAA89210. Ref.3
Sequence conflict13541K → M in AAC97879. Ref.2
Sequence conflict14381A → V in BAA89210. Ref.3

Secondary structure

......... 1483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 0CC146FEBB954261

FASTA1,483170,903
        10         20         30         40         50         60 
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 

        70         80         90        100        110        120 
THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC 

       130        140        150        160        170        180 
DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKETVV 

       190        200        210        220        230        240 
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 

       250        260        270        280        290        300 
LIRTERPPNK EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 

       310        320        330        340        350        360 
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP LKVKNSKNSK 

       370        380        390        400        410        420 
SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK PLKAKGRSKG ILNGQKSTGN 

       430        440        450        460        470        480 
SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRTSSKPHKH LPPAALHLIA 

       490        500        510        520        530        540 
YYKENKDRED KRSALSCVIS KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE 

       550        560        570        580        590        600 
EQRKEYLKKK REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 

       610        620        630        640        650        660 
GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ 

       670        680        690        700        710        720 
TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD VQEESEGSDT DDNKDSAAFE 

       730        740        750        760        770        780 
DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER 

       790        800        810        820        830        840 
LAVLKEENDK KRAEKQKRKE MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS 

       850        860        870        880        890        900 
AVKSRRLLAI QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR 

       910        920        930        940        950        960 
TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE DYCPRSKKAN 

       970        980        990       1000       1010       1020 
LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL DELLNCLHPQ GIRESQLKER 

      1030       1040       1050       1060       1070       1080 
LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYVEETSEF 

      1090       1100       1110       1120       1130       1140 
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV 

      1150       1160       1170       1180       1190       1200 
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 

      1210       1220       1230       1240       1250       1260 
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA SEDSEDDESD 

      1270       1280       1290       1300       1310       1320 
EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR SGRRPGKKPH STRRSQPKAP 

      1330       1340       1350       1360       1370       1380 
PVDDAEVDEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF SWPFREPVTR DEAEDYYDVI 

      1390       1400       1410       1420       1430       1440 
THPMDFQTVQ NKCSCGSYRS VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL 

      1450       1460       1470       1480 
HKHLPGHPYV RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK 

« Hide

Isoform 2 [UniParc].

Checksum: D0F1A5559EB52F78
Show »

FASTA1,479170,447

References

« Hide 'large scale' references
[1]"Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23."
Peoples R.J., Cisco M.J., Kaplan P., Francke U.
Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A novel human gene, WSTF, is deleted in Williams Syndrome."
Lu X., Meng X., Morris C.A., Keating M.T.
Genomics 54:241-249(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN WBS.
[3]"A novel family of bromodomain genes."
Jones M.H., Hamana N., Nezu J., Shimane M.
Genomics 63:40-45(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[7]"WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci."
Bozhenok L., Wade P.A., Varga-Weisz P.
EMBO J. 21:2231-2241(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[9]"The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci."
Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.
Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
[10]"Ligand-induced transrepression by VDR through association of WSTF with acetylated histones."
Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.
EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VDR, DOMAIN BROMO.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX.
[13]"Identification of novel human Cdt1-binding proteins by a proteomics approach: proteolytic regulation by APC/CCdh1."
Sugimoto N., Kitabayashi I., Osano S., Tatsumi Y., Yugawa T., Narisawa-Saito M., Matsukage A., Kiyono T., Fujita M.
Mol. Biol. Cell 19:1007-1021(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-374; SER-699; SER-705; SER-708; SER-716; SER-947; SER-1315 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity."
Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., Elledge S.J., Allis C.D.
Nature 457:57-62(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF CYS-338.
[18]"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-345; SER-347; SER-349; SER-361; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-349; SER-705; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor."
Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E.
J. Mol. Biol. 304:723-729(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1185-1235.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084479 mRNA. Translation: AAD08675.1.
AF072810 mRNA. Translation: AAC97879.1. Frameshift.
AB032253 mRNA. Translation: BAA89210.1. Frameshift.
AC005074 Genomic DNA. Translation: AAD04720.1. Sequence problems.
AC005089 Genomic DNA. Translation: AAP22332.1.
CH471200 Genomic DNA. Translation: EAW69680.1.
CH471200 Genomic DNA. Translation: EAW69681.1.
BC065029 mRNA. Translation: AAH65029.1. Sequence problems.
BC136520 mRNA. Translation: AAI36521.1.
RefSeqNP_115784.1. NM_032408.3.
UniGeneHs.743372.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F62NMR-A1185-1235[»]
ProteinModelPortalQ9UIG0.
SMRQ9UIG0. Positions 1181-1458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114497. 48 interactions.
DIPDIP-35642N.
IntActQ9UIG0. 9 interactions.
MINTMINT-1894324.
STRING9606.ENSP00000342434.

PTM databases

PhosphoSiteQ9UIG0.

Polymorphism databases

DMDM22653670.

Proteomic databases

PaxDbQ9UIG0.
PRIDEQ9UIG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339594; ENSP00000342434; ENSG00000009954. [Q9UIG0-1]
ENST00000404251; ENSP00000385442; ENSG00000009954. [Q9UIG0-1]
ENST00000573731; ENSP00000461849; ENSG00000262694. [Q9UIG0-1]
ENST00000575505; ENSP00000460410; ENSG00000262694. [Q9UIG0-1]
GeneID9031.
KEGGhsa:9031.
UCSCuc003tyc.3. human. [Q9UIG0-1]

Organism-specific databases

CTD9031.
GeneCardsGC07M072854.
HGNCHGNC:961. BAZ1B.
HPACAB037081.
CAB037158.
MIM605681. gene.
neXtProtNX_Q9UIG0.
Orphanet904. Williams syndrome.
PharmGKBPA25271.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOVERGENHBG050668.
InParanoidQ9UIG0.
KOK11658.
OMADEDYCPR.
OrthoDBEOG72G17K.
PhylomeDBQ9UIG0.
TreeFamTF106397.

Gene expression databases

BgeeQ9UIG0.
CleanExHS_BAZ1B.
GenevestigatorQ9UIG0.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
IPR013136. WSTF_Acf1_Cbp146.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAZ1B. human.
EvolutionaryTraceQ9UIG0.
GeneWikiBAZ1B.
GenomeRNAi9031.
NextBio33835.
PROQ9UIG0.
SOURCESearch...

Entry information

Entry nameBAZ1B_HUMAN
AccessionPrimary (citable) accession number: Q9UIG0
Secondary accession number(s): B9EGK3 expand/collapse secondary AC list , D3DXE9, O95039, O95247, O95277, Q6P1K4, Q86UJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 30, 2002
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM